Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Video

Updated: Jun 26, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Evidence that alpha-synuclein does not inhibit phospholipase D.

Irit Rappley1, Aaron D Gitler, Paige E Selvy

  • 1Department of Neurology, Harvard Medical School and Brigham & Women's Hospital, Boston, Massachusetts 02115, USA.

Biochemistry
|January 17, 2009
PubMed
Summary

Alpha-synuclein (alphaSyn) does not directly inhibit phospholipase D (PLD). Previous findings suggesting this interaction may stem from cellular stress caused by alphaSyn overexpression, not a direct biochemical function.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Lower plasma resolvin D1 level and greater sputum eosinophilia characterize a cluster of severe asthma patients.

Respiratory research·2026
Same author

Polyunsaturated fatty acids modulation of smoking-related epigenetics and pulmonary outcomes.

Genes & nutrition·2026
Same author

An emergent disease-associated motor neuron state precedes cell death in ALS.

Cell·2026
Same author

Sustained Reduction in Cardiopulmonary Fitness in Long COVID: A Report from the RECOVER-adult Cohort Study.

JACC. Advances·2026
Same author

Cryptic splicing in synaptic and membrane excitability genes links TDP-43 loss to neuronal dysfunction.

Science translational medicine·2026
Same author

The Unusual Suspects.

The New England journal of medicine·2026

Area of Science:

  • Neuroscience
  • Biochemistry
  • Cell Biology

Background:

  • Alpha-synuclein (alphaSyn) is a brain-enriched protein genetically linked to Parkinson's disease (PD).
  • AlphaSyn aggregates form the characteristic Lewy bodies in PD.
  • Previous studies suggested alphaSyn inhibits phospholipase D (PLD) activity.

Purpose of the Study:

  • To investigate the direct interaction between alpha-synuclein and phospholipase D.
  • To determine if alphaSyn inhibits PLD activity in various experimental systems.

Main Methods:

  • Cell-free assays using purified proteins.
  • Mammalian cell lines to assess endogenous and overexpressed PLD inhibition.
  • Yeast models to examine PLD-dependent phenotypes.

More Related Videos

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
09:44

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Related Experiment Videos

Last Updated: Jun 26, 2026

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays
09:36

Recombinant α- β- and γ-Synucleins Stimulate Protein Phosphatase 2A Catalytic Subunit Activity in Cell Free Assays

Published on: August 13, 2017

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo
09:44

Generation of Alpha-Synuclein Preformed Fibrils from Monomers and Use In Vivo

Published on: June 2, 2019

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

Main Results:

  • No significant inhibition of PLD by alphaSyn was observed in cell-free assays.
  • AlphaSyn did not inhibit endogenous or overexpressed PLD in mammalian cells.
  • No direct interaction between alphaSyn and PLD was detected across tested systems.

Conclusions:

  • The proposed inhibitory effect of alphaSyn on PLD is unlikely to be a direct biochemical function.
  • Reported effects may be an indirect consequence of endoplasmic reticulum stress from alphaSyn overexpression.
  • This study refutes a direct functional link between alphaSyn and PLD activity.